LRP_ECOL6
ID LRP_ECOL6 Reviewed; 164 AA.
AC P0ACJ1; P19494;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Leucine-responsive regulatory protein;
GN Name=lrp; OrderedLocusNames=c1026;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Mediates a global response to leucine. Exogenous leucine
CC affects the expression of a number of different operons; lrp mediates
CC this effect for at least some of these operons. For example it is
CC regulator of the branched-chain amino acid transport genes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN79498.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN79498.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000228473.1; NC_004431.1.
DR AlphaFoldDB; P0ACJ1; -.
DR BMRB; P0ACJ1; -.
DR SMR; P0ACJ1; -.
DR STRING; 199310.c1026; -.
DR EnsemblBacteria; AAN79498; AAN79498; c1026.
DR GeneID; 67414649; -.
DR KEGG; ecc:c1026; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_091233_0_0_6; -.
DR OMA; AGDENYI; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProt.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR PRINTS; PR00033; HTHASNC.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS00519; HTH_ASNC_1; 1.
DR PROSITE; PS50956; HTH_ASNC_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..164
FT /note="Leucine-responsive regulatory protein"
FT /id="PRO_0000111730"
FT DOMAIN 12..73
FT /note="HTH asnC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT DNA_BIND 31..50
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
SQ SEQUENCE 164 AA; 18887 MW; 2952FB9347A2725C CRC64;
MVDSKKRPGK DLDRIDRNIL NELQKDGRIS NVELSKRVGL SPTPCLERVR RLERQGFIQG
YTALLNPHYL DASLLVFVEI TLNRGAPDVF EQFNTAVQKL EEIQECHLVS GDFDYLLKTR
VPDMSAYRKL LGETLLRLPG VNDTRTYVVM EEVKQSNRLV IKTR